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1 Texas A&M University System Health Science Center, Institute of Biosciences and Technology, Center for Extracellular Matrix Biology, Houston, TX 77030, USA
2 University of Texas Medical School, Division of Infectious Diseases, Department of Internal Medicine, and Department of Microbiology and Molecular Genetics, Center for the Study of Emerging and Re-emerging Pathogens (CERP), Houston, TX 77030, USA
Correspondence
Magnus Höök
mhook{at}ibt.tamushsc.edu
The recently published Enterococcus faecalis genome [Paulsen, I. T., Banerjei, L., Myers, G. S. & 29 other authors (2003). Science 299, 2071–2074)] was examined and 41 putative cell-wall-anchored proteins were identified. Seventeen of these proteins are predicted to contain tandemly repeated immunoglobulin-like folds characteristic of the structural organization of staphylococcal adhesins of the MSCRAMM (microbial surface component recognizing adhesive matrix molecules) type. Two of the nine proteins selected for further study appear to represent cell-wall-anchored enzymes. It is proposed that the remaining seven proteins constitute a family of structurally related proteins potentially interacting with proteins of the host. This family includes the previously identified collagen/laminin-binding MSCRAMM ACE [Rich, R. L., Kreikemeyer, B., Owens, R. T., LaBrenz, S., Narayana, S. V., Weinstock, G. M., Murray, B. E. & Hook, M. (1999). J Biol Chem 274, 26939–26945]. It is further demonstrated that genes encoding the seven putative MSCRAMMs are present in all E. faecalis strains tested and these proteins appear to be expressed during infection in humans, since sera from infected individuals contain antibodies reacting with recombinant versions of the enterococcal proteins.
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